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Tetragonal crystal structure of TAS3 C-terminal alpha motif

Analyse Tetragonal crystal structure of TAS3 C-terminal alpha motif in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3D1B
Type
protein
Length
327 residues
Chains
3
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
RNA-induced transcriptional silencing complex protein TAS3
UniProt
O94687
Pockets
1 · best druggability 0.73

Structure

x-ray diffraction · 2 distinct chains · 72% helix, 2% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ARNA-induced transcriptional silencing complex protein TAS3protein11172% helix, 2% strandO94687
B, CRNA-induced transcriptional silencing complex protein TAS3protein10872% helix, 2% strandO94687

Pockets

1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
19070.730.7778empty

Interfaces

3 interfaces between chains.

  • A–B · 587 Ų buried · 9 hydrogen bonds · protein-protein
  • B–C · 576 Ų buried · 6 hydrogen bonds · protein-protein
  • A–C · 146 Ų buried · 1 hydrogen bond · protein-protein

Compared structures

  • 3D1B · Tetragonal crystal structure of Tas3 C-terminal alpha motif · the same entry in another collection · chain B against B, TM-score 1.00
  • O94687 · AlphaFold monomer V2.0 prediction for RNA-induced transcriptional silencing complex… · a predicted model of the same protein · chain A against A, TM-score 0.99

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